Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

Q74MX2 (AGOG_NANEQ) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 52. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
N-glycosylase/DNA lyase
Alternative name(s):
8-oxoguanine DNA glycosylase
EC=3.2.2.-
AGOG
DNA-(apurinic or apyrimidinic site) lyase
Short name=AP lyase
EC=4.2.99.18
Gene names
Ordered Locus Names:NEQ515
OrganismNanoarchaeum equitans (strain Kin4-M) [Reference proteome] [HAMAP]
Taxonomic identifier228908 [NCBI]
Taxonomic lineageArchaeaNanoarchaeotaNanoarchaeum

Protein attributes

Sequence length216 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

DNA repair enzyme that is part of the base excision repair (BER) pathway; protects from oxidative damage by removing the major product of DNA oxidation, 8-oxoguanine (GO), from single- and double-stranded DNA substrates By similarity. HAMAP-Rule MF_01168

Catalytic activity

The C-O-P bond 3' to the apurinic or apyrimidinic site in DNA is broken by a beta-elimination reaction, leaving a 3'-terminal unsaturated sugar and a product with a terminal 5'-phosphate. HAMAP-Rule MF_01168

Domain

Contains two alpha-helical subdomains, with the 8-oxoguanine binding site located in a cleft at their interface. Contains a helix-hairpin-helix (HhH) structural motif and a Gly/Pro-rich sequence followed by a conserved Asp (HhH-GPD motif). HAMAP-Rule MF_01168

Sequence similarities

Belongs to the archaeal N-glycosylase/DNA lyase (AGOG) family.

Ontologies

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 216216N-glycosylase/DNA lyase HAMAP-Rule MF_01168
PRO_0000185111

Regions

Region106 – 17065Helix-hairpin-helix HAMAP-Rule MF_01168

Sites

Active site1301Schiff-base intermediate with DNA By similarity
Active site1621 Potential
Binding site2718-oxoguanine By similarity
Binding site4818-oxoguanine; via carbonyl oxygen By similarity
Binding site5918-oxoguanine By similarity
Binding site13418-oxoguanine By similarity
Binding site16018-oxoguanine; via carbonyl oxygen By similarity
Binding site19018-oxoguanine By similarity
Binding site19418-oxoguanine By similarity

Sequences

Sequence LengthMass (Da)Tools
Q74MX2 [UniParc].

Last modified July 5, 2004. Version 1.
Checksum: DC1D0C211503B3FA

FASTA21626,005
        10         20         30         40         50         60 
MEDPLIKILK QFSIEDAKYV EYNLDRQFLA LKENPKPVGL VIANALISYQ LTMPGERYWE 

        70         80         90        100        110        120 
LFAKKVNSFN DLYDFVKKYN PRFLSNKLKR LERFKPYIDI IEQNREHYYE NMVALNKFLA 

       130        140        150        160        170        180 
KIMNQNIYDK TIVFSIKMFA YAMRALGYKF KPFPFEIAIP LDYRLKKINP DLNYWFYVSK 

       190        200        210 
QTNIPPLHID SLIWPIFRIK NLPKKFALLK EYLSNL 

« Hide

References

[1]"The genome of Nanoarchaeum equitans: insights into early archaeal evolution and derived parasitism."
Waters E., Hohn M.J., Ahel I., Graham D.E., Adams M.D., Barnstead M., Beeson K.Y., Bibbs L., Bolanos R., Keller M., Kretz K., Lin X., Mathur E., Ni J., Podar M., Richardson T., Sutton G.G., Simon M. expand/collapse author list , Soell D., Stetter K.O., Short J.M., Noorderwier M.
Proc. Natl. Acad. Sci. U.S.A. 100:12984-12988(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Kin4-M.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE017199 Genomic DNA. Translation: AAR39356.1.
RefSeqNP_963795.1. NC_005213.1.

3D structure databases

ProteinModelPortalQ74MX2.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING228908.NEQ515.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAR39356; AAR39356; NEQ515.
GeneID2654177.
KEGGneq:NEQ515.

Phylogenomic databases

eggNOGCOG4047.
HOGENOMHOG000254352.
KOK01741.
OMAREHYYEN.

Enzyme and pathway databases

BioCycNEQU228908:GJB6-543-MONOMER.

Family and domain databases

Gene3D1.10.1670.10. 1 hit.
1.10.340.30. 1 hit.
HAMAPMF_01168. AGOG.
InterProIPR011257. DNA_glycosylase.
IPR023170. HTH_base_excis_C.
IPR015254. N-Glyclase/DNA_lyase-like_arc.
IPR016544. N-Glyclase/DNA_lyase_arc.
[Graphical view]
PfamPF09171. DUF1886. 1 hit.
[Graphical view]
PIRSFPIRSF008955. AGOG. 1 hit.
SUPFAMSSF48150. SSF48150. 1 hit.
ProtoNetSearch...

Entry information

Entry nameAGOG_NANEQ
AccessionPrimary (citable) accession number: Q74MX2
Entry history
Integrated into UniProtKB/Swiss-Prot: January 10, 2006
Last sequence update: July 5, 2004
Last modified: May 14, 2014
This is version 52 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families